BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Chapter 32, Problem 3P
Interpretation Introduction
Interpretation:
The expected number of times an 8 bp, 10 bp, and 12bp DNA site would be present in E. Coli, should be calculated.
Concept introduction:
The building block of DNA and RNA is termed as the
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2. For the flow of fluid over a flat membrane of length 10cm,
determine the length-average mass transfer coefficient. The
relevant properties of the system are u=0.01cm²/s, D=5 x 106
cm²/s, and v = 5.0 cm/s.
Background
Freezing isn't the only challenge in cryopreservation - thawing can
be just as difficult. A microwave oven seems like a nice solution,
since it deposits energy quickly and microwaves are non-ionizing
radiation (they do not cause DNA mutation). However, water
absorbs microwaves more effectively than ice does, meaning that
the portion of an organ that has already melted will get warmer at a
higher rate than the remaining ice – the opposite of what we want!
-
The transmission of radiation through a weakly absorbing material
such as ice or water can be modeled by Beer's law, which assumes
that the rate of absorption at a depth x is proportional to the local
radiation intensity I(x) times an absorption coefficient, which is often
written as μ or a or just µ). Noting that absorption decreases the
intensity, we can write a differential equation
a
Solving the differential equation with the boundary condition on the
surface being
gives the relationship
For a standard microwave oven…
3. Dry air is inhaled at a rate of 10 liter/min through a trachea with
a diameter of 20 mm and a length of 125 mm. The inner
surface of the trachea is at a normal body temperature of 37°C
and may be assumed to be saturated with water.
a. Assuming steady, fully developed flow in the trachea,
estimate the mass transfer convection coefficient.
b. Estimate the daily water loss (liter/day) associated with
evaporation in the trachea.
Chapter 32 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
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- For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?arrow_forwardAssume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?arrow_forwardAn enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0 kcal/mol. Calulate the catalytic power at 310K. (R-1.987x10 kcal/mol)arrow_forward
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